Effects of high pressure on meat: A review.

High pressure induced changes on sarcoplasmic protein fraction and quality indicators.

High hydrostatic pressure (HHP) treatment can influence meat protein conformation and induce protein denaturation, aggregation, or gelation. The means whereby HHP treatment exerts effects on meat protein structure change are due to the rupture of noncovalent interactions within protein molecules, and to the subsequent re-formation of intra- and inter-molecular bonds within or among protein molecules. Depending upon the meat protein system, the pressure, the temperature, and the duration of the pressure treatment, meat can be either tenderized or toughened. Muscle texture variation induced by heat treatment is due to breakage of hydrogen bonds, whereas changes from high pressure treatment are due to the rupture of hydrophobic and electrostatic interactions. Pressure treatment has little effect on the toughness of connective tissue. Juiciness, springiness, and chewiness are increased upon HHP treatment. Prerigor HHP treatment tenderizes meat, whereas tenderizing effects of postrigor HHP treatment are only measureable if pressure and heat treatment are combined. The limitations and future applications of high pressure technology are also discussed.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1750-3841.2009.01449.x

High hydrostatic pressure effects on the texture of meat and meat products

Methods were investigated to reduce the salt content of beef-containing smallgoods as high-salt intake has been identified as a public health risk for most individuals. Raw meat batters were manufactured from retail beef mince (4–7% fat) using various NaCl concentrations (0–2%), and were packed into casings and subjected to high pressure processing (up to 400 MPa for 2 min at 10 °C). Following pressure treatment, samples were cooked to an internal temperature of 72 °C and cooled. Cooked products were assessed for cooking loss, colour and physical consistency by texture profile analysis. Flavour and overall acceptability were assessed by sensory panels. High pressure processing (HPP) was found to produce a dramatic improvement in the moisture retention of the cooked products. Control (unpressurised) sausages containing 2% NaCl had a similar cook loss (9.3%) to pressure-treated sausages containing just 1% NaCl, whereas unpressurised samples with 1% NaCl had a cook loss of 24.9%. The hardness and gumminess of pressure-treated samples was higher compared to untreated samples, at all salt concentrations. The greatest differences in texture with pressure treatment were seen in the 1% NaCl samples. Pressure treatment generally caused no changes in the colour of either the raw or cooked product; however there was a slight increase in “whiteness” with pressure treatment. Sensory panels reported a greater acceptability in both appearance and texture of pressure-treated sausages of lower salt content compared with non-pressure-treated samples. Examination of extracted proteins using SDS-PAGE and of muscle proteins by thermal analysis indicated that pressure contributed to enhanced binding through protein solubilisation and gelation through partial protein unfolding. The application of high pressure to beef sausages with low-salt content resulted in reduced cooking losses and improved texture. Industrial relevance Enhanced meat binding through extraction of salt-soluble proteins is an essential step in the formulation of meat products such as sausages and emulsion-type products. The ability to reduce salt and achieve high binding and water retention through use of HPP is important in being able to produce healthier foods.

Use of high pressure to reduce cook loss and improve texture of low-salt beef sausage batters

Studies of the effect of hydrostatic pressure pretreatment on thermal gelation of chicken myofibrils and pork meat patty

In an earlier study it was found that the application of high pressure to homogenates of meat in saline solution could increase water-holding capacity and promote the solubilization of proteins. These studies have now been extended to myofibrils prepared from sheep semimembrano-sus muscle. The amount of protein solubilized by pressurization was found to be dependent on (1) temperature, generally being greater at 0°C than at 30°C; (2) the nature and the concentration of the salt; and (3) the pH. SDS gel electrophoresis indicated that solubilization of all the major constituent proteins of the myofibril could be promoted. It is suggested that the imidazole group is implicated in the pressure solubilization effect.

I. J. McKENZIE

Papers

Pressure-induced solubilization of myofibrillar proteins